ID   ALR_ALCBS               Reviewed;         353 AA.
AC   Q0VMG4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Alanine racemase;
DE            EC=5.1.1.1;
GN   Name=alr; OrderedLocusNames=ABO_2186;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: Provides the D-alanine required for cell wall
CC       biosynthesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
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DR   EMBL; AM286690; CAL17634.1; -; Genomic_DNA.
DR   RefSeq; YP_693906.1; -.
DR   GeneID; 4213284; -.
DR   GenomeReviews; AM286690_GR; ABO_2186.
DR   KEGG; abo:ABO_2186; -.
DR   NMPDR; fig|393595.12.peg.2186; -.
DR   HOGENOM; Q0VMG4; -.
DR   OMA; Q0VMG4; TGLKPAM.
DR   BioCyc; ABOR393595:ABO_2186-MON; -.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:HAMAP.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_01201; -; 1.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR000821; Ala_racemase_reg.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; FALSE_NEG.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Complete proteome;
KW   Isomerase; Peptidoglycan synthesis; Pyridoxal phosphate.
FT   CHAIN         1    353       Alanine racemase.
FT                                /FTId=PRO_1000065968.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine
FT                                (By similarity).
FT   ACT_SITE    251    251       Proton acceptor; specific for L-alanine
FT                                (By similarity).
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   353 AA;  37526 MW;  7CBBC19C326EAA06 CRC64;
     MRGTRVEIRL AALRNNALRA AELAGDAQVF AMVKANGYGH GLLLAAETML DSVSGLGVAV
     LDEARTLREH GIALPILVAE GFFDAEELEA AARLSLEVVV HSLWQVELLL ANPCPVRIWL
     KVNAGMNRLG LRPNEALSAA ARLSQAGNAP VGVMSHFACA DMDEDIHSEK QLLLAGSVAE
     QLQLPLSASN SAALLRYPRA HAQRVRPGIM LYGSSPFNWQ TAAELGLQVS HRFSARLIAI
     NAVEAGESVG YGATWTASDP RQIGVVAVGY GDGYPRHAPS GTPVAVNGVV TTLVGRVSMD
     MITIDVTGLS ASVGDEVELW GDVVDVDDVA RACGTISYEL FCQITQRPER TIV
//